Functions of unique middle loop and C-terminal tail in GnT-III activity and secretion

• Published in: Biochimica et biophysica acta. General subjects Vol. 1869; no. 1; p. 130734
• Main Authors: Bao, WanXue, Yamasaki, Takahiro, Nakano, Miyako, Nagae, Masamichi, Kizuka, Yasuhiko
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.01.2025
• Subjects: Animals; Disordered segment; Glycosylation; Glycosyltransferase; GnT-III (MGAT3); HEK293 Cells; Humans; N-Acetylglucosaminyltransferases - genetics; N-Acetylglucosaminyltransferases - metabolism; N-glycan; Polysaccharides - metabolism; Protein Domains; SSA; GnT-III (MGAT3); CBB; KO; Glycosyltransferase; Disordered segment; LC-ESI MS; PHA; DAPI; Glycosylation; GnT; ER; DMEM; RCA; CHX; FBS; N-glycan; WT

N-Glycan branching modulates the diversity of protein functions. β1,4-N-acetylglucosaminyltransferase III (GnT-III or MGAT3) produces a unique GlcNAc branch, “bisecting GlcNAc”, in N-glycans, and is involved in Alzheimer's disease and cancer. However, the 3D structure and catalytic mechanism of...